ID   GGAP_SPITZ              Reviewed;         587 AA.
AC   G0GBS4;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Glucosylglycerate phosphorylase {ECO:0000303|PubMed:28754708};
DE            Short=GGa phosphorylase {ECO:0000303|PubMed:28754708};
DE            Short=GGaP {ECO:0000303|PubMed:28754708};
DE            EC=2.4.1.352 {ECO:0000269|PubMed:28754708};
GN   OrderedLocusNames=Spith_0877 {ECO:0000312|EMBL:AEJ61152.1};
OS   Spirochaeta thermophila (strain ATCC 700085 / DSM 6578 / Z-1203).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Spirochaeta.
OX   NCBI_TaxID=869211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700085 / DSM 6578 / Z-1203;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikailova N., Pagani I.,
RA   Chertkov O., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Merkhoffer B., Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Spirochaeta thermophila DSM 6578.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=28754708; DOI=10.1128/aem.01434-17;
RA   Franceus J., Pinel D., Desmet T.;
RT   "Glucosylglycerate phosphorylase, an enzyme with novel specificity involved
RT   in compatible solute metabolism.";
RL   Appl. Environ. Microbiol. 83:0-0(2017).
CC   -!- FUNCTION: Catalyzes the reversible phosphorolysis of glucosylglycerate
CC       into alpha-D-glucose 1-phosphate (Glc1P) and D-glycerate. May be a
CC       regulator of intracellular levels of glucosylglycerate, a compatible
CC       solute that primarily protects organisms facing salt stress and very
CC       specific nutritional constraints. Cannot catalyze the phosphorolysis of
CC       sucrose. {ECO:0000269|PubMed:28754708}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + phosphate = (R)-
CC         glycerate + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:55268,
CC         ChEBI:CHEBI:16659, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601,
CC         ChEBI:CHEBI:62510; EC=2.4.1.352;
CC         Evidence={ECO:0000269|PubMed:28754708};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.8 mM for D-glycerate (at pH 6.5 and 42 degrees Celsius)
CC         {ECO:0000269|PubMed:28754708};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       Glucosylglycerate phosphorylase subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002903; AEJ61152.1; -; Genomic_DNA.
DR   RefSeq; WP_014624526.1; NC_017583.1.
DR   AlphaFoldDB; G0GBS4; -.
DR   SMR; G0GBS4; -.
DR   STRING; 869211.Spith_0877; -.
DR   EnsemblBacteria; AEJ61152; AEJ61152; Spith_0877.
DR   KEGG; stq:Spith_0877; -.
DR   HOGENOM; CLU_021358_0_0_12; -.
DR   OMA; PNATQFT; -.
DR   OrthoDB; 1573900at2; -.
DR   Proteomes; UP000007254; Chromosome.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11356; AmyAc_Sucrose_phosphorylase-like_1; 1.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 3.90.400.10; -; 1.
DR   InterPro; IPR033746; GGa_phosphorylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR045857; O16G_dom_2.
DR   InterPro; IPR016377; Sucrose_GGa_phosphorylase-rel.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   PIRSF; PIRSF003059; Sucrose_phosphorylase; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..587
FT                   /note="Glucosylglycerate phosphorylase"
FT                   /id="PRO_0000442434"
FT   ACT_SITE        236
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:A0ZZH6"
SQ   SEQUENCE   587 AA;  67022 MW;  8B7D63A3E6765F16 CRC64;
     MEPVDRMREL LSFIYGPETG RDTHEALHAL LDGWRGRLPS PDEEYASGRL PLDHTDAVLI
     TYGDQFGRKG EAPLATLGEF LREYLSGTMK GVHILPFFPY SSDDGFSVMD YRRVNPEWGT
     WDDVRRISED FRLMVDLVLN HCSAKSEWFR RFLQGDPEYE DFFITVEPGT DLSGVFRPRA
     LPLVHEFESA KGPVLVWTTF SRDQVDLNYA NPRVLLEMID IFLFYVSQGA QIIRLDAIAY
     LWKELGTPCI HHPKTHAVVK LFRAICEEVC PWVLIITETN VPHKENISYF GDMDEAHLVY
     QFALPPLVLD AFLRKDVSYL REWARTIDTY GGKVSYFNFL ASHDGIGVLP ARGILPDEYI
     DAMIEAVKDR GGLISYKSTP QGEVPYELNI NYLSAISESH LDRPTRARKF LASQAVMLSL
     VGMPGIYVHS LLGSENWREG VEKTGMNRTI NRQKLSYEGV LEELRDPESL RSMVFEGYLD
     MLAARRKSRA FDPRGMQEVL EAPETVFALL RRSPDATEEV LCLINVSHIE QECVFPSSIF
     RTAPDAHLFT ELTSGDTLVP YREDEDRFSI SLGGYEVLWL TPYRDKG